Ligand binding in the catalytic antibody 17E8. A free energy perturbation calculation study

Thomas Fox, Thomas S. Scanlan, Peter A. Kollman

Research output: Contribution to journalArticlepeer-review

37 Scopus citations

Abstract

We present free energy calculations on the Michaelis complexes of the catalytic antibody 17E8 with two substrates, which differ only in their side chains. Replacing a -CH2- group with a -S- increases K(M) by a factor of about 5-8. This corresponds to a free energy 'preference' for the -CH2- ligand of about 0.9-1.3 kcal/mol. The calculations semiquantitatively reproduce the experimental free energies and show that the preference for a -CH2- over a -S- is mainly due to the more favorable solvation free energy in the unbound form of the molecule.

Original languageEnglish (US)
Pages (from-to)11571-11577
Number of pages7
JournalJournal of the American Chemical Society
Volume119
Issue number48
DOIs
StatePublished - Dec 1 1997

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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